Glucose Transport System - We will attempt to purify the uptake protein after its separation from the binding factor. There are indications it might be a glycoprotein. We would like to try and modify the membrane vesicle preparations in such a way that we may be able to enclose an energizing system into them and thereby convert the enhanced diffusion into an accumulation process as seen with the living cell. Nucleotide Polyphosphates - An attempt will be made to isolate relaxed mutants from B. brevis in order to study the physiological roles of the two enzymes. We will also study the mechanism of control of ppGpp degradation with the purified ppGpp-hydrolyzing enzyme, and investigate the point of cAMP inhibition in yeast metabolism as well as the mechanism of methionine reversal of this inhibition. We will try to find pyrophosphate 3'-CoA in cellular extracts and check other CoA-linked reactions for the possibility of replacing the normal with the pyrophosphate 3'-compound. We will test with a new enzyme other 3'-phosphate-containing coenzymes as acceptors of pyrophosphate, probably using the active sulfate 3'-phosphoadenosine-5'-phosphosulfate.